ArticleThe Journal of biological chemistry
Cross-seeding of alpha-synuclein aggregation by amyloid fibrils of food proteins.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 49 citations in OpenAlex.
- Controlling interfacial protein adsorption, desorption and aggregation in biomolecular condensates.Nature communications · 2025Article
- Amyloid Cross-Interactions through the Lens of Simulations: The Case of Aβ-IAPP.The journal of physical chemistry. B · 2025Article
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- The Promising Role of Selenium and Yeast in the Fight Against Protein Amyloidosis.Biological trace element research · 2025Review
- In Vitro Cell Model Investigation of Alpha-Synuclein Aggregate Morphology Using Spectroscopic Imaging.International journal of molecular sciences · 2024Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Amyloidogenic propensity of self-assembling peptides and their adjuvant potential for use as DNA vaccines.Acta biomaterialia · 2023Article
- Coaggregation of polyglutamine (polyQ) proteins is mediated by polyQ-tract interactions and impairs cellular proteostasis.Acta biochimica et biophysica Sinica · 2023Article
- Quantitative Seed Amplification Assay: A Proof-of-Principle Study.The journal of physical chemistry. B · 2023Article
- Food protein-derived amyloids do not accelerate amyloid β aggregation.Scientific reports · 2023Article
- Real-Time Fast Amyloid Seeding and Translocation of α-Synuclein with a Nanopipette.ACS central science · 2022Article
- Interactions between SARS-CoV-2 N-Protein and α-Synuclein Accelerate Amyloid Formation.ACS chemical neuroscience · 2022Article
- Microbiome Impact on Amyloidogenesis.Frontiers in molecular biosciences · 2022Review
- AA amyloid in human food chain is a possible biohazard.Scientific reports · 2021Article
- Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aggregation of the protein α-synuclein (aSyn) into amyloid fibrils in the human brain is associated with the development of several neurodegenerative diseases, including Parkinson's disease. The previously observed prion-like spreading of aSyn aggregation throughout the brain and the finding that heterologous cross-seeding of amyloid aggregation occurs in vitro for some proteins suggest that exposure to amyloids in general may pose a risk for disease development. To elucidate which protein fibril characteristics determine if and how heterologous amyloid seeding can occur, we investigated the potential of amyloid fibrils formed from proteins found in food, hen egg white lysozyme, and bovine milk β-lactoglobulin to cross-seed aSyn aggregation in the test tube. We observed that amyloid fibrils from lysozyme, but not β-lactoglobulin, potently cross-seeded the aggregation of aSyn as indicated by a significantly shorter lag phase of aSyn aggregation in the presence of lysozyme fibrils. The cross-seeding effect of lysozyme was found to be primarily driven by a surface-mediated nucleation mechanism. The differential seeding effect of lysozyme and β-lactoglobulin on aSyn aggregation could be explained on the basis of binding affinity, binding site, and electrostatic interactions. Our results indicate that heterologous seeding of proteins may occur depending on the physicochemical characteristics of the seed protein fibril. Our findings suggest that heterologous seeding has the potential to determine the pathogenesis of neurodegenerative amyloid diseases.
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